FB2026_01 , released March 12, 2026
FB2026_01 , released March 12, 2026
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Renfranz, P.J., Beckerle, M.C. (2002). Doing (F/L)PPPPs: EVH1 domains and their proline-rich partners in cell polarity and migration.  Curr. Opin. Cell Biol. 14(1): 88--103.
FlyBase ID
FBrf0151636
Publication Type
Review
Abstract
Actin filament assembly is a tightly regulated process that functions in many aspects of cell physiology. Members of the Ena/VASP (Drosophila Enabled/vasodilator-stimulated phosphoprotein) family are key players in regulating actin filament assembly, in many cases through their association with binding partners that display a particular proline-rich motif, FPPPP. Ena/VASP proteins interact with these partners via the highly conserved Ena/VASP homology 1 (EVH1) domain. The diverse array of binding partners for EVH1 domains, including cytoskeletal proteins such as zyxin, transmembrane guidance receptors such as Roundabout, and the T-cell signaling protein Fyb/SLAP, shows that these interactions are likely to be important in a number of cellular processes that require regulated actin filament assembly.
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Curr. Opin. Cell Biol.
    Title
    Current Opinion in Cell Biology
    Publication Year
    1989-
    ISBN/ISSN
    0955-0674
    Data From Reference
    Genes (13)